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Absence of phosphoglucose isomerase-1 in retinal photoreceptor, pigment epithelium and Muller cells

Archer, SN; Ahuja Jensen, Poonam LU ; Caffé, Romeo LU ; Mikol, C; Foster, RG; van Veen, Theo LU and von Schantz, M (2004) In European Journal of Neuroscience 19(11). p.2923-2930
Abstract
Macroarray analysis was used to compare equal amounts of cDNA from wild-type and rd/rd (retinal degeneration) mice, collected at P90 when photoreceptor degeneration is virtually complete. A stronger signal for the glycolytic enzyme phosphoglucose isomerase (Gpi1) was observed in the rd/rd sample. Extracellularly, Gpi1 may act as a cytokine, independently described as neuroleukin and autocrine motility factor. Retinal Gpi1 expression was investigated by Northern and Western blot analysis and immunohistochemistry. Double-labelling was performed with antibodies against Gpi1 and calbindin-D, glutamine synthetase, RPE65, calretinin and ultraviolet opsin in order to provide positive cell type identification. Northern and Western blots showed... (More)
Macroarray analysis was used to compare equal amounts of cDNA from wild-type and rd/rd (retinal degeneration) mice, collected at P90 when photoreceptor degeneration is virtually complete. A stronger signal for the glycolytic enzyme phosphoglucose isomerase (Gpi1) was observed in the rd/rd sample. Extracellularly, Gpi1 may act as a cytokine, independently described as neuroleukin and autocrine motility factor. Retinal Gpi1 expression was investigated by Northern and Western blot analysis and immunohistochemistry. Double-labelling was performed with antibodies against Gpi1 and calbindin-D, glutamine synthetase, RPE65, calretinin and ultraviolet opsin in order to provide positive cell type identification. Northern and Western blots showed double expression levels per microgram of RNA and protein, respectively, in the rd/rd retina compared with wild-type. However, the total amount of Gpi1 protein per retina was indistinguishable. Gpi1 immunoreactivity was found in ganglion, amacrine, horizontal and bipolar cells, but not in rods, cones, pigment epithelium and Muller cells. This distribution explains why the absolute amounts of Gpi1 protein were not appreciably different between wild-type and the rd/rd phenotype, where rods and cones are absent, whilst the relative contribution of Gpi1 to the total protein and RNA pools differed. Some extracellular immunoreactivity was observed in the photoreceptor matrix around cones in freshly fixed tissue only, which could possibly reflect a role as a cytokine. We propose that glycolysis in Gpi1-negative cells proceeds entirely through the pentose phosphate pathway, creating NADPH at the cost of organic carbon. We hypothesize that the unique metabolic needs of photoreceptors justify this trade-off. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
pentose phosphate pathway, glycolysis, mouse, photoreceptor metabolism
in
European Journal of Neuroscience
volume
19
issue
11
pages
2923 - 2930
publisher
Wiley-Blackwell
external identifiers
  • wos:000221789800002
  • pmid:15182299
  • scopus:3042606350
ISSN
1460-9568
DOI
10.1111/j.1460-9568.2004.03417.x
language
English
LU publication?
yes
id
f1403c86-fcad-479b-aa46-e42c358f495c (old id 276637)
date added to LUP
2007-08-02 10:12:28
date last changed
2017-10-08 03:39:21
@article{f1403c86-fcad-479b-aa46-e42c358f495c,
  abstract     = {Macroarray analysis was used to compare equal amounts of cDNA from wild-type and rd/rd (retinal degeneration) mice, collected at P90 when photoreceptor degeneration is virtually complete. A stronger signal for the glycolytic enzyme phosphoglucose isomerase (Gpi1) was observed in the rd/rd sample. Extracellularly, Gpi1 may act as a cytokine, independently described as neuroleukin and autocrine motility factor. Retinal Gpi1 expression was investigated by Northern and Western blot analysis and immunohistochemistry. Double-labelling was performed with antibodies against Gpi1 and calbindin-D, glutamine synthetase, RPE65, calretinin and ultraviolet opsin in order to provide positive cell type identification. Northern and Western blots showed double expression levels per microgram of RNA and protein, respectively, in the rd/rd retina compared with wild-type. However, the total amount of Gpi1 protein per retina was indistinguishable. Gpi1 immunoreactivity was found in ganglion, amacrine, horizontal and bipolar cells, but not in rods, cones, pigment epithelium and Muller cells. This distribution explains why the absolute amounts of Gpi1 protein were not appreciably different between wild-type and the rd/rd phenotype, where rods and cones are absent, whilst the relative contribution of Gpi1 to the total protein and RNA pools differed. Some extracellular immunoreactivity was observed in the photoreceptor matrix around cones in freshly fixed tissue only, which could possibly reflect a role as a cytokine. We propose that glycolysis in Gpi1-negative cells proceeds entirely through the pentose phosphate pathway, creating NADPH at the cost of organic carbon. We hypothesize that the unique metabolic needs of photoreceptors justify this trade-off.},
  author       = {Archer, SN and Ahuja Jensen, Poonam and Caffé, Romeo and Mikol, C and Foster, RG and van Veen, Theo and von Schantz, M},
  issn         = {1460-9568},
  keyword      = {pentose phosphate pathway,glycolysis,mouse,photoreceptor metabolism},
  language     = {eng},
  number       = {11},
  pages        = {2923--2930},
  publisher    = {Wiley-Blackwell},
  series       = {European Journal of Neuroscience},
  title        = {Absence of phosphoglucose isomerase-1 in retinal photoreceptor, pigment epithelium and Muller cells},
  url          = {http://dx.doi.org/10.1111/j.1460-9568.2004.03417.x},
  volume       = {19},
  year         = {2004},
}